5h03: Difference between revisions
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==Crystal structure of an ADP-ribosylating toxin BECa from C. perfringens== | |||
<StructureSection load='5h03' size='340' side='right' caption='[[5h03]], [[Resolution|resolution]] 1.89Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5h03]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H03 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H03 FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h04|5h04]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5h03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h03 OCA], [http://pdbe.org/5h03 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h03 RCSB], [http://www.ebi.ac.uk/pdbsum/5h03 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h03 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Binary enterotoxin of Clostridium perfringens (BEC), consisting of the components BECa and BECb, was recently identified as a novel enterotoxin produced by C. perfringens that causes acute gastroenteritis in humans. Although the detailed mechanism of cell intoxication by BEC remains to be defined, BECa shows both NAD+-glycohydrolase and actin ADP-ribosyltransferase activities in the presence of NAD+. In this study, we determined the first crystal structure of BECa in its apo-state and in complex with NADH. The structure of BECa shows striking resemblance with other binary actin ADP-ribosylating toxins (ADPRTs), especially in terms of its overall protein fold and mechanisms of substrate recognition. We present a detailed picture of interactions between BECa and NADH, including bound water molecules located near the C1'-N glycosidic bond of NADH and the catalytically important ADP-ribosylating turn-turn (ARTT) loop. We observed that the conformational rearrangement of the ARTT loop, possibly triggered by a conformational change involving a conserved tyrosine residue coupled with substrate binding, plays a crucial role in catalysis by properly positioning a catalytic glutamate residue in the E-X-E motif of the ARTT loop in contact with the nucleophile. Our results for BECa provide insight into the common catalytic mechanism of the family of binary actin ADPRTs. | |||
Crystal structure of the ADP-ribosylating component of BEC, the binary enterotoxin of Clostridium perfringens.,Kawahara K, Yonogi S, Munetomo R, Oki H, Yoshida T, Kumeda Y, Matsuda S, Kodama T, Ohkubo T, Iida T, Nakamura S Biochem Biophys Res Commun. 2016 Nov 11;480(2):261-267. doi:, 10.1016/j.bbrc.2016.10.042. Epub 2016 Oct 15. PMID:27751850<ref>PMID:27751850</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5h03" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Iida, T]] | |||
[[Category: Kawahara, K]] | |||
[[Category: Kodama, T]] | |||
[[Category: Kumeda, Y]] | |||
[[Category: Matsuda, S]] | |||
[[Category: Munetomo, R]] | |||
[[Category: Nakamura, S]] | |||
[[Category: Ohkubo, T]] | |||
[[Category: Oki, H]] | |||
[[Category: Yonogi, S]] | |||
[[Category: Yoshida, T]] | |||
[[Category: Adp-ribosyltransferase]] | |||
[[Category: Toxin]] | |||
